| Literature DB >> 21526763 |
Alba T Macias1, Douglas S Williamson, Nicola Allen, Jenifer Borgognoni, Alexandra Clay, Zoe Daniels, Pawel Dokurno, Martin J Drysdale, Geraint L Francis, Christopher J Graham, Rob Howes, Natalia Matassova, James B Murray, Rachel Parsons, Terry Shaw, Allan E Surgenor, Lindsey Terry, Yikang Wang, Mike Wood, Andrew J Massey.
Abstract
78 kDa glucose-regulated protein (Grp78) is a heat shock protein (HSP) involved in protein folding that plays a role in cancer cell proliferation. Binding of adenosine-derived inhibitors to Grp78 was characterized by surface plasmon resonance and isothermal titration calorimetry. The most potent compounds were 13 (VER-155008) with K(D) = 80 nM and 14 with K(D) = 60 nM. X-ray crystal structures of Grp78 bound to ATP, ADPnP, and adenosine derivative 10 revealed differences in the binding site between Grp78 and homologous proteins.Entities:
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Year: 2011 PMID： 21526763 DOI： 10.1021/jm101625x
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446